Evidence map›Paper›PMID 28009842›Full record

ReviewMolecules (Basel, Switzerland)2016

Sulfur Atom in its Bound State Is a Unique Element Involved in Physiological Functions in Mammals.

Shin Koike, Yuki Ogasawara

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Sulfur Administration in Fe-S Cluster Homeostasis.Antioxidants (Basel, Switzerland) · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Chemical Biology of HChemical reviews · 2018
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Sulphurous Mineral Waters: New Applications for Health.Evidence-based complementary and alternative medicine : eCAM · 2017
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Shin KoikeDepartment of Analytical Biochemistry, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose, Tokyo 204-8588, Japan. skoike@my-pharm.ac.jp.
Yuki OgasawaraDepartment of Analytical Biochemistry, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose, Tokyo 204-8588, Japan. yo@my-pharm.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It was in the 1950s that the term polysulfide or persulfide was introduced in biological studies. The unfamiliar term "sulfane sulfur" sometimes appeared in papers published in the 1970s, and was defined in the review article by Westley in 1983. In the article, sulfane sulfur is described as sulfur atoms that are covalently bound only with sulfur atoms, and as this explanation was somewhat difficult to comprehend, it was not generally accepted. Thus, in the early 1990s, we redefined these sulfur species as "bound sulfur", which easily converts to hydrogen sulfide on reduction with a thiol reducing agent. In other words, bound sulfur refers to a sulfur atom that exists in a zero to divalent form (0 to -2). The first part of this review focuses on the fluorescent derivatization HPLC method-which we developed for measurement of bound sulfur-and explains the distribution of bound sulfur and the hydrogen sulfide-producing ability of various tissues, as clarified by this method. Next, we discuss diverse physiological functions and involvement of polysulfide, a typical type of bound sulfur, in the redox regulation system. Additionally, we also address its possible physiological role in the central nervous system, based on its action of scavenging reactive carbonyl compounds.

Indexed as

AnimalsCentral Nervous SystemCysteineGene Expression RegulationGlycation End Products, AdvancedHydrogen SulfideIron-Sulfur ProteinsKelch-Like ECH-Associated Protein 1MammalsNF-E2-Related Factor 2Oxidation-ReductionOxidative StressPhosphatidylinositol 3-KinasesSignal TransductionSulfidesSulfurCysteineGlycation End Products, AdvancedHydrogen SulfideIron-Sulfur ProteinsKEAP1 protein, humanKelch-Like ECH-Associated Protein 1NFE2L2 protein, humanNF-E2-Related Factor 2persulfidesPhosphatidylinositol 3-KinasespolysulfideSulfidesSulfurbound sulfurhydrogen sulfideoxidative stresspersulfidepolysulfides

Identifiers

PMID28009842
PMCPMC6273515

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.